Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15025

- TNIP1_HUMAN

UniProt

Q15025 - TNIP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

TNFAIP3-interacting protein 1

Gene

TNIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection.5 Publications

GO - Molecular functioni

  1. mitogen-activated protein kinase binding Source: UniProtKB

GO - Biological processi

  1. defense response Source: ProtInc
  2. glycoprotein biosynthetic process Source: UniProtKB
  3. inflammatory response Source: UniProtKB-KW
  4. leukocyte cell-cell adhesion Source: UniProtKB
  5. modulation by symbiont of host I-kappaB kinase/NF-kappaB cascade Source: UniProtKB
  6. MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
  7. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  8. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  9. negative regulation of viral genome replication Source: UniProtKB
  10. positive regulation of inflammatory response Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. translation Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Inflammatory response

Names & Taxonomyi

Protein namesi
Recommended name:
TNFAIP3-interacting protein 1
Alternative name(s):
A20-binding inhibitor of NF-kappa-B activation 1
Short name:
ABIN-1
HIV-1 Nef-interacting protein
Nef-associated factor 1
Short name:
Naf1
Nip40-1
Virion-associated nuclear shuttling protein
Short name:
VAN
Short name:
hVAN
Gene namesi
Name:TNIP1
Synonyms:KIAA0113, NAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:16903. TNIP1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. intracellular Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi472 – 4721D → N: Abolishes binding to polyubiquitin ('K-63'-linked and linear). 1 Publication
Mutagenesisi552 – 5521Y → F: Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit. 1 Publication

Organism-specific databases

Orphaneti536. Systemic lupus erythematosus.
PharmGKBiPA128394573.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636TNFAIP3-interacting protein 1PRO_0000096691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei403 – 4031Phosphoserine3 Publications
Modified residuei438 – 4381Phosphothreonine1 Publication
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei552 – 5521Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15025.
PaxDbiQ15025.
PRIDEiQ15025.

PTM databases

PhosphoSiteiQ15025.

Expressioni

Tissue specificityi

Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain. In peripheral blood mononucleocytes, isoform 4 is mainly expressed and isoform 1 and isoform 7 are almost not expressed. Expression of isoform 1 and isoform 7 increases in leukemic cells.1 Publication

Gene expression databases

BgeeiQ15025.
CleanExiHS_NAF1.
HS_TNIP1.
ExpressionAtlasiQ15025. baseline and differential.
GenevestigatoriQ15025.

Organism-specific databases

HPAiHPA037893.
HPA037894.

Interactioni

Subunit structurei

Interacts with TNFAIP3 and IKBKG (polyubiquitinated); facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex. Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri ipah9.8; the interaction promotes polyubiquitination of IKBKG.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNG1P519594EBI-357849,EBI-3905829
GIT2Q141613EBI-357849,EBI-1046878
IKBKGQ9Y6K94EBI-357849,EBI-81279
ipaH9.8Q8VSC34EBI-357849,EBI-6125799From a different organism.
MAGEB18Q96M612EBI-357849,EBI-741835
OPTNQ96CV93EBI-357849,EBI-748974

Protein-protein interaction databases

BioGridi115602. 39 interactions.
DIPiDIP-27577N.
IntActiQ15025. 31 interactions.
MINTiMINT-200912.
STRINGi9606.ENSP00000317891.

Structurei

3D structure databases

ProteinModelPortaliQ15025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 412319Interacts with NefAdd
BLAST
Regioni351 – 36717Interaction with Shigella flexneri ipah9.8Add
BLAST
Regioni431 – 588158Required for inhibitory activity of TNF-induced NF-kappa-B activationBy similarityAdd
BLAST
Regioni452 – 51059Ubiquitin-binding domain (UBD)Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili20 – 7354Sequence AnalysisAdd
BLAST
Coiled coili196 – 25863Sequence AnalysisAdd
BLAST
Coiled coili294 – 535242Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi524 – 5307Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi539 – 63698Pro-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG120932.
GeneTreeiENSGT00510000046908.
HOGENOMiHOG000253048.
HOVERGENiHBG019072.
InParanoidiQ15025.
OMAiNQSSQVM.
OrthoDBiEOG7SJD44.
PhylomeDBiQ15025.
TreeFamiTF351138.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q15025-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha, FL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE
60 70 80 90 100
ESQMEATRLR QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP
110 120 130 140 150
TAPACPSDKP APVQKPPSSG TSSEFEVVTP EEQNSPESSS HANAMALGPL
160 170 180 190 200
PREDGNLMLH LQRLETTLSV CAEEPDHGQL FTHLGRMALE FNRLASKVHK
210 220 230 240 250
NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL REENLELKKL
260 270 280 290 300
LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE
310 320 330 340 350
KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT
360 370 380 390 400
DLEAEREQKQ RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD
410 420 430 440 450
QLSPLTRQRE YQEKEIQRLN KALEEALSIQ TPPSSPPTAF GSPEGAGALL
460 470 480 490 500
RKQELVTQNE LLKQQVKIFE EDFQRERSDR ERMNEEKEEL KKQVEKLQAQ
510 520 530 540 550
VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH PEHLCGAYPY
560 570 580 590 600
AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL
610 620 630
PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ
Length:636
Mass (Da):71,864
Last modified:August 1, 1999 - v2
Checksum:iD81B96BEAD50D871
GO
Isoform 2 (identifier: Q15025-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     627-636: SPKNDREGPQ → PADLRLPRN

Show »
Length:635
Mass (Da):71,788
Checksum:iFE65D2CE6E7B185B
GO
Isoform 3 (identifier: Q15025-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Show »
Length:583
Mass (Da):66,012
Checksum:iA97F0EB85F9F39DE
GO
Isoform 4 (identifier: Q15025-4) [UniParc]FASTAAdd to Basket

Also known as: Alpha2

The sequence of this isoform differs from the canonical sequence as follows:
     530-593: Missing.

Show »
Length:572
Mass (Da):64,500
Checksum:iD1E76C1FBBA59E63
GO
Isoform 5 (identifier: Q15025-5) [UniParc]FASTAAdd to Basket

Also known as: Alpha4

The sequence of this isoform differs from the canonical sequence as follows:
     530-556: ASGERYHVEPHPEHLCGAYPYAYPPMP → SLQKMTVRGLSETRLCHLAPPSSCRAS
     557-636: Missing.

Note: Less effective in the NF-kappa-B inhibitory effect.

Show »
Length:556
Mass (Da):62,609
Checksum:i757B3E9B83C35F42
GO
Isoform 6 (identifier: Q15025-6) [UniParc]FASTAAdd to Basket

Also known as: Beta2

The sequence of this isoform differs from the canonical sequence as follows:
     530-593: Missing.
     627-636: SPKNDREGPQ → PADLRLPRN

Show »
Length:571
Mass (Da):64,424
Checksum:i929F73D89B3D0A54
GO
Isoform 7 (identifier: Q15025-7) [UniParc]FASTAAdd to Basket

Also known as: Alpha3, Beta3

The sequence of this isoform differs from the canonical sequence as follows:
     530-545: ASGERYHVEPHPEHLC → GTHRGCPRRLPERKVK
     546-636: Missing.

Show »
Length:545
Mass (Da):61,570
Checksum:i7F4AD5363F28608B
GO
Isoform 8 (identifier: Q15025-8) [UniParc]FASTAAdd to Basket

Also known as: Beta4

The sequence of this isoform differs from the canonical sequence as follows:
     530-552: ASGERYHVEPHPEHLCGAYPYAY → SQLISDCQETRSHLHGVARASAG
     553-636: Missing.

Show »
Length:552
Mass (Da):62,103
Checksum:i699AD04365381366
GO

Sequence cautioni

The sequence AAB41438.1 differs from that shown. Reason: Frameshift at positions 152 and 154. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481G → D in AAH12133. (PubMed:15489334)Curated
Sequence conflicti178 – 1781G → S in BAH13185. (PubMed:14702039)Curated
Sequence conflicti299 – 2991A → P in AAG42154. (PubMed:11090181)Curated
Sequence conflicti299 – 2991A → P in BAF34946. (PubMed:17016622)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031P → S.
Corresponds to variant rs2303018 [ dbSNP | Ensembl ].
VAR_051453
Natural varianti146 – 1461A → V.
Corresponds to variant rs2233289 [ dbSNP | Ensembl ].
VAR_051454
Natural varianti151 – 1511P → A.
Corresponds to variant rs2233290 [ dbSNP | Ensembl ].
VAR_051455
Natural varianti233 – 2331R → Q.
Corresponds to variant rs2233292 [ dbSNP | Ensembl ].
VAR_051456
Natural varianti260 – 2601A → V.
Corresponds to variant rs2233295 [ dbSNP | Ensembl ].
VAR_051457
Natural varianti263 – 2631R → W in patients with gastrointestinal diffuse large cell lymphoma. 1 Publication
Corresponds to variant rs117663772 [ dbSNP | Ensembl ].
VAR_067965
Natural varianti286 – 2861T → M in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation. 1 Publication
Corresponds to variant rs185683917 [ dbSNP | Ensembl ].
VAR_067966
Natural varianti374 – 3741I → T in patients with gastrointestinal diffuse large cell lymphoma. 1 Publication
VAR_067967
Natural varianti476 – 4761E → K in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation. 1 Publication
VAR_067968

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353Missing in isoform 3. 3 PublicationsVSP_045296Add
BLAST
Alternative sequencei530 – 59364Missing in isoform 4 and isoform 6. 1 PublicationVSP_055208Add
BLAST
Alternative sequencei530 – 55627ASGER…YPPMP → SLQKMTVRGLSETRLCHLAP PSSCRAS in isoform 5. 1 PublicationVSP_055209Add
BLAST
Alternative sequencei530 – 55223ASGER…YPYAY → SQLISDCQETRSHLHGVARA SAG in isoform 8. 1 PublicationVSP_055210Add
BLAST
Alternative sequencei530 – 54516ASGER…PEHLC → GTHRGCPRRLPERKVK in isoform 7. 1 PublicationVSP_055211Add
BLAST
Alternative sequencei546 – 63691Missing in isoform 7. 1 PublicationVSP_055212Add
BLAST
Alternative sequencei553 – 63684Missing in isoform 8. 1 PublicationVSP_055213Add
BLAST
Alternative sequencei557 – 63680Missing in isoform 5. 1 PublicationVSP_055214Add
BLAST
Alternative sequencei627 – 63610SPKNDREGPQ → PADLRLPRN in isoform 2 and isoform 6. 3 PublicationsVSP_003913

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011895 mRNA. Translation: CAA09855.1.
AJ011896 mRNA. Translation: CAA09856.1.
AY012155 mRNA. Translation: AAG42154.1.
AB177543 mRNA. Translation: BAF34946.1.
AB177544 mRNA. Translation: BAF34947.1.
AB252970 mRNA. Translation: BAF48787.1.
AB252971 mRNA. Translation: BAF48788.1.
AB252972 mRNA. Translation: BAF48789.1.
AB252973 mRNA. Translation: BAF48790.1.
AB252974 mRNA. Translation: BAF48791.1.
AB252975 mRNA. Translation: BAF48792.1.
AB252976 mRNA. Translation: BAF48793.1.
AB252977 mRNA. Translation: BAF48794.1.
AB252978 mRNA. Translation: BAF48795.1.
AB252979 mRNA. Translation: BAF48796.1.
AB252980 mRNA. Translation: BAF48797.1.
AB252981 mRNA. Translation: BAF48798.1.
D30755 mRNA. Translation: BAA06416.2.
AK299975 mRNA. Translation: BAH13185.1.
BX640647 mRNA. Translation: CAE45793.1.
AC008641 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61688.1.
CH471062 Genomic DNA. Translation: EAW61689.1.
CH471062 Genomic DNA. Translation: EAW61690.1.
CH471062 Genomic DNA. Translation: EAW61691.1.
BC012133 mRNA. Translation: AAH12133.1.
BC014008 mRNA. Translation: AAH14008.1.
U39403 mRNA. Translation: AAC99999.1.
U83844 mRNA. Translation: AAB41438.1. Frameshift.
CCDSiCCDS34280.1. [Q15025-1]
CCDS58982.1. [Q15025-3]
CCDS58983.1. [Q15025-5]
CCDS58984.1. [Q15025-4]
CCDS58985.1. [Q15025-2]
RefSeqiNP_001239314.1. NM_001252385.1.
NP_001239315.1. NM_001252386.1. [Q15025-3]
NP_001239319.1. NM_001252390.1. [Q15025-1]
NP_001239320.1. NM_001252391.1. [Q15025-1]
NP_001239321.1. NM_001252392.1. [Q15025-2]
NP_001239322.1. NM_001252393.1. [Q15025-2]
NP_001245383.1. NM_001258454.1. [Q15025-1]
NP_001245384.1. NM_001258455.1. [Q15025-4]
NP_001245385.1. NM_001258456.1. [Q15025-5]
NP_006049.3. NM_006058.4. [Q15025-1]
XP_006714814.1. XM_006714751.1. [Q15025-4]
XP_006714815.1. XM_006714752.1. [Q15025-6]
UniGeneiHs.355141.
Hs.731557.

Genome annotation databases

EnsembliENST00000315050; ENSP00000317891; ENSG00000145901. [Q15025-1]
ENST00000518977; ENSP00000430971; ENSG00000145901. [Q15025-2]
ENST00000520931; ENSP00000429891; ENSG00000145901. [Q15025-3]
ENST00000521591; ENSP00000430760; ENSG00000145901. [Q15025-1]
ENST00000522226; ENSP00000428187; ENSG00000145901. [Q15025-1]
ENST00000523200; ENSP00000431105; ENSG00000145901. [Q15025-4]
ENST00000523338; ENSP00000428243; ENSG00000145901. [Q15025-2]
ENST00000524280; ENSP00000429912; ENSG00000145901. [Q15025-5]
ENST00000610535; ENSP00000483944; ENSG00000145901. [Q15025-4]
ENST00000610874; ENSP00000484665; ENSG00000145901. [Q15025-5]
GeneIDi10318.
KEGGihsa:10318.
UCSCiuc003ltg.4. human. [Q15025-1]
uc003ltk.3. human.

Polymorphism databases

DMDMi20138952.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011895 mRNA. Translation: CAA09855.1 .
AJ011896 mRNA. Translation: CAA09856.1 .
AY012155 mRNA. Translation: AAG42154.1 .
AB177543 mRNA. Translation: BAF34946.1 .
AB177544 mRNA. Translation: BAF34947.1 .
AB252970 mRNA. Translation: BAF48787.1 .
AB252971 mRNA. Translation: BAF48788.1 .
AB252972 mRNA. Translation: BAF48789.1 .
AB252973 mRNA. Translation: BAF48790.1 .
AB252974 mRNA. Translation: BAF48791.1 .
AB252975 mRNA. Translation: BAF48792.1 .
AB252976 mRNA. Translation: BAF48793.1 .
AB252977 mRNA. Translation: BAF48794.1 .
AB252978 mRNA. Translation: BAF48795.1 .
AB252979 mRNA. Translation: BAF48796.1 .
AB252980 mRNA. Translation: BAF48797.1 .
AB252981 mRNA. Translation: BAF48798.1 .
D30755 mRNA. Translation: BAA06416.2 .
AK299975 mRNA. Translation: BAH13185.1 .
BX640647 mRNA. Translation: CAE45793.1 .
AC008641 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61688.1 .
CH471062 Genomic DNA. Translation: EAW61689.1 .
CH471062 Genomic DNA. Translation: EAW61690.1 .
CH471062 Genomic DNA. Translation: EAW61691.1 .
BC012133 mRNA. Translation: AAH12133.1 .
BC014008 mRNA. Translation: AAH14008.1 .
U39403 mRNA. Translation: AAC99999.1 .
U83844 mRNA. Translation: AAB41438.1 . Frameshift.
CCDSi CCDS34280.1. [Q15025-1 ]
CCDS58982.1. [Q15025-3 ]
CCDS58983.1. [Q15025-5 ]
CCDS58984.1. [Q15025-4 ]
CCDS58985.1. [Q15025-2 ]
RefSeqi NP_001239314.1. NM_001252385.1.
NP_001239315.1. NM_001252386.1. [Q15025-3 ]
NP_001239319.1. NM_001252390.1. [Q15025-1 ]
NP_001239320.1. NM_001252391.1. [Q15025-1 ]
NP_001239321.1. NM_001252392.1. [Q15025-2 ]
NP_001239322.1. NM_001252393.1. [Q15025-2 ]
NP_001245383.1. NM_001258454.1. [Q15025-1 ]
NP_001245384.1. NM_001258455.1. [Q15025-4 ]
NP_001245385.1. NM_001258456.1. [Q15025-5 ]
NP_006049.3. NM_006058.4. [Q15025-1 ]
XP_006714814.1. XM_006714751.1. [Q15025-4 ]
XP_006714815.1. XM_006714752.1. [Q15025-6 ]
UniGenei Hs.355141.
Hs.731557.

3D structure databases

ProteinModelPortali Q15025.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115602. 39 interactions.
DIPi DIP-27577N.
IntActi Q15025. 31 interactions.
MINTi MINT-200912.
STRINGi 9606.ENSP00000317891.

PTM databases

PhosphoSitei Q15025.

Polymorphism databases

DMDMi 20138952.

Proteomic databases

MaxQBi Q15025.
PaxDbi Q15025.
PRIDEi Q15025.

Protocols and materials databases

DNASUi 10318.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315050 ; ENSP00000317891 ; ENSG00000145901 . [Q15025-1 ]
ENST00000518977 ; ENSP00000430971 ; ENSG00000145901 . [Q15025-2 ]
ENST00000520931 ; ENSP00000429891 ; ENSG00000145901 . [Q15025-3 ]
ENST00000521591 ; ENSP00000430760 ; ENSG00000145901 . [Q15025-1 ]
ENST00000522226 ; ENSP00000428187 ; ENSG00000145901 . [Q15025-1 ]
ENST00000523200 ; ENSP00000431105 ; ENSG00000145901 . [Q15025-4 ]
ENST00000523338 ; ENSP00000428243 ; ENSG00000145901 . [Q15025-2 ]
ENST00000524280 ; ENSP00000429912 ; ENSG00000145901 . [Q15025-5 ]
ENST00000610535 ; ENSP00000483944 ; ENSG00000145901 . [Q15025-4 ]
ENST00000610874 ; ENSP00000484665 ; ENSG00000145901 . [Q15025-5 ]
GeneIDi 10318.
KEGGi hsa:10318.
UCSCi uc003ltg.4. human. [Q15025-1 ]
uc003ltk.3. human.

Organism-specific databases

CTDi 10318.
GeneCardsi GC05M150409.
HGNCi HGNC:16903. TNIP1.
HPAi HPA037893.
HPA037894.
MIMi 607714. gene.
neXtProti NX_Q15025.
Orphaneti 536. Systemic lupus erythematosus.
PharmGKBi PA128394573.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG120932.
GeneTreei ENSGT00510000046908.
HOGENOMi HOG000253048.
HOVERGENi HBG019072.
InParanoidi Q15025.
OMAi NQSSQVM.
OrthoDBi EOG7SJD44.
PhylomeDBi Q15025.
TreeFami TF351138.

Miscellaneous databases

ChiTaRSi TNIP1. human.
GeneWikii TNIP1.
GenomeRNAii 10318.
NextBioi 35461715.
PROi Q15025.
SOURCEi Search...

Gene expression databases

Bgeei Q15025.
CleanExi HS_NAF1.
HS_TNIP1.
ExpressionAtlasi Q15025. baseline and differential.
Genevestigatori Q15025.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and cloning of a novel cellular protein Naf1, Nef-associated factor 1, that increases cell surface CD4 expression."
    Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J., Yamamoto N.
    FEBS Lett. 442:83-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Peripheral blood.
  2. "A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions."
    Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.
    J. Virol. 74:11811-11824(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Leukocyte.
  3. "Multiple splicing variants of Naf1/ABIN-1 transcripts and their alterations in hematopoietic tumors."
    Shiote Y., Ouchida M., Jitsumori Y., Ogama Y., Matsuo Y., Ishimaru F., Tanimoto M., Shimizu K.
    Int. J. Mol. Med. 18:917-923(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, FUNCTION.
  4. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Colon endothelium.
  8. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  11. "Transcriptional map of the Treacher Collins candidate gene region."
    Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
    Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2).
    Tissue: Craniofacial.
  12. Fukushi M., Kimura T., Yamamoto N.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
  13. Cited for: FUNCTION, INTERACTION WITH MAPK1.
  14. "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
    Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
    J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKG AND TNFAIP3.
  15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "P-selectin primes leukocyte integrin activation during inflammation."
    Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y., Zhu X., Plow E.F., Chen M., Geng J.G.
    Nat. Immunol. 8:882-892(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT TYR-552, MUTAGENESIS OF TYR-552.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response."
    Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.
    Nat. Cell Biol. 12:66-73(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, MUTAGENESIS OF 476-GLU-ARG-477.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF ASP-472.
  24. "A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma."
    Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y., Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S., Srivastava G., Du M.Q.
    Clin. Cancer Res. 17:1440-1451(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.

Entry informationi

Entry nameiTNIP1_HUMAN
AccessioniPrimary (citable) accession number: Q15025
Secondary accession number(s): A4F1W8
, A4F1W9, A4F1X2, A4F1X4, A4F1X5, A4F1X6, A4F1X7, A4F1X9, B7Z699, E7EPY1, E7ET96, O76008, Q05KP3, Q05KP4, Q6N077, Q96EL9, Q99833, Q9H1J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: August 1, 1999
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3